HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 21-DEC-18 6NGY
TITLE STRUCTURE OF RAT NEURONAL NITRIC OXIDE SYNTHASE HEME DOMAIN IN COMPLEX
TITLE 2 WITH (R)-6-(2,3-DIFLUORO-5-(2-(1-METHYLPYRROLIDIN-2-YL)ETHYL)
TITLE 3 PHENETHYL)-4-METHYLPYRIDIN-2-AMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NITRIC OXIDE SYNTHASE, BRAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BNOS,CONSTITUTIVE NOS,NC-NOS,NOS TYPE I,NEURONAL NOS,NNOS,
COMPND 5 PEPTIDYL-CYSTEINE S-NITROSYLASE NOS1;
COMPND 6 EC: 1.14.13.39;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 GENE: NOS1, BNOS;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PCWORI
KEYWDS NITRIC OXIDE SYNTHASE INHIBITOR COMPLEX HEME ENZYME, OXIDOREDUCTASE,
KEYWDS 2 OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.LI,T.L.POULOS
REVDAT 4 11-OCT-23 6NGY 1 LINK
REVDAT 3 04-DEC-19 6NGY 1 REMARK
REVDAT 2 27-MAR-19 6NGY 1 JRNL
REVDAT 1 13-MAR-19 6NGY 0
JRNL AUTH H.T.DO,H.LI,G.CHREIFI,T.L.POULOS,R.B.SILVERMAN
JRNL TITL OPTIMIZATION OF BLOOD-BRAIN BARRIER PERMEABILITY WITH POTENT
JRNL TITL 2 AND SELECTIVE HUMAN NEURONAL NITRIC OXIDE SYNTHASE
JRNL TITL 3 INHIBITORS HAVING A 2-AMINOPYRIDINE SCAFFOLD.
JRNL REF J. MED. CHEM. V. 62 2690 2019
JRNL REFN ISSN 1520-4804
JRNL PMID 30802056
JRNL DOI 10.1021/ACS.JMEDCHEM.8B02032
REMARK 2
REMARK 2 RESOLUTION. 1.93 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1-2575_1496: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.93
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.050
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 71610
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 6772
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.0078 - 5.9847 1.00 4398 214 0.1475 0.1554
REMARK 3 2 5.9847 - 4.7529 1.00 4318 258 0.1380 0.1989
REMARK 3 3 4.7529 - 4.1529 1.00 4403 251 0.1257 0.1493
REMARK 3 4 4.1529 - 3.7735 1.00 4365 222 0.1343 0.1954
REMARK 3 5 3.7735 - 3.5033 1.00 4338 256 0.1477 0.1980
REMARK 3 6 3.5033 - 3.2968 1.00 4367 228 0.1696 0.1780
REMARK 3 7 3.2968 - 3.1318 1.00 4420 196 0.1923 0.2657
REMARK 3 8 3.1318 - 2.9955 1.00 4355 252 0.2159 0.2436
REMARK 3 9 2.9955 - 2.8802 1.00 4348 243 0.2059 0.2516
REMARK 3 10 2.8802 - 2.7809 1.00 4370 237 0.2080 0.2578
REMARK 3 11 2.7809 - 2.6939 1.00 4378 209 0.2210 0.2481
REMARK 3 12 2.6939 - 2.6170 1.00 4379 208 0.2264 0.3046
REMARK 3 13 2.6170 - 2.5481 0.99 4350 232 0.2313 0.2804
REMARK 3 14 2.5481 - 2.4859 1.00 4356 221 0.2374 0.2925
REMARK 3 15 2.4859 - 2.4294 1.00 4411 227 0.2567 0.3547
REMARK 3 16 2.4294 - 2.3777 0.99 4311 232 0.2379 0.3388
REMARK 3 17 2.3777 - 2.3302 1.00 4390 194 0.2460 0.3003
REMARK 3 18 2.3302 - 2.2862 1.00 4348 245 0.2553 0.3055
REMARK 3 19 2.2862 - 2.2454 1.00 4308 289 0.2646 0.3135
REMARK 3 20 2.2454 - 2.2073 0.99 4369 223 0.2816 0.3420
REMARK 3 21 2.2073 - 2.1717 0.99 4272 225 0.2845 0.3740
REMARK 3 22 2.1717 - 2.1383 0.99 4421 200 0.2934 0.4140
REMARK 3 23 2.1383 - 2.1069 0.99 4358 176 0.3102 0.3812
REMARK 3 24 2.1069 - 2.0772 0.99 4330 210 0.3157 0.3832
REMARK 3 25 2.0772 - 2.0491 0.99 4377 247 0.3095 0.3802
REMARK 3 26 2.0491 - 2.0225 0.99 4338 219 0.3105 0.3328
REMARK 3 27 2.0225 - 1.9972 0.99 4299 208 0.3215 0.3821
REMARK 3 28 1.9972 - 1.9732 0.97 4296 215 0.3475 0.4065
REMARK 3 29 1.9732 - 1.9502 0.96 4145 256 0.3683 0.4571
REMARK 3 30 1.9502 - 1.9283 0.78 3440 179 0.3750 0.4458
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.810
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 7125
REMARK 3 ANGLE : 0.983 9691
REMARK 3 CHIRALITY : 0.050 1003
REMARK 3 PLANARITY : 0.006 1220
REMARK 3 DIHEDRAL : 17.311 4153
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 299:716)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.3269 4.7719 22.5551
REMARK 3 T TENSOR
REMARK 3 T11: 0.2654 T22: 0.3050
REMARK 3 T33: 0.3188 T12: 0.0088
REMARK 3 T13: 0.0070 T23: -0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 1.0050 L22: 1.5129
REMARK 3 L33: 7.5394 L12: -0.2433
REMARK 3 L13: -0.4036 L23: -0.2964
REMARK 3 S TENSOR
REMARK 3 S11: -0.0584 S12: 0.1087 S13: -0.0182
REMARK 3 S21: 0.0779 S22: -0.0770 S23: 0.0790
REMARK 3 S31: -0.0491 S32: -0.3914 S33: 0.1028
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 299:718)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3192 5.0148 59.8926
REMARK 3 T TENSOR
REMARK 3 T11: 0.2208 T22: 0.2683
REMARK 3 T33: 0.3179 T12: -0.0034
REMARK 3 T13: 0.0414 T23: 0.0330
REMARK 3 L TENSOR
REMARK 3 L11: 1.0327 L22: 1.3034
REMARK 3 L33: 3.7512 L12: -0.1754
REMARK 3 L13: -0.0444 L23: 0.6299
REMARK 3 S TENSOR
REMARK 3 S11: 0.0007 S12: -0.0106 S13: 0.0908
REMARK 3 S21: -0.1522 S22: -0.0719 S23: -0.0463
REMARK 3 S31: 0.0668 S32: 0.1687 S33: 0.0602
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6NGY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1000236865.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-NOV-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 300K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72182
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.928
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 11.40
REMARK 200 R MERGE (I) : 0.17600
REMARK 200 R SYM (I) : 0.17600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.99
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.90
REMARK 200 R MERGE FOR SHELL (I) : 5.78900
REMARK 200 R SYM FOR SHELL (I) : 5.78900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 1OM4
REMARK 200
REMARK 200 REMARK: BRICKS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-24% PEG3350, 0.1M MES 0.14-0.20M
REMARK 280 AMMONIUM ACETATE, 10% ETHYLENE GLYCOL, 30UM SDS, 5 MM GSH, PH
REMARK 280 5.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 25.92150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 82.14250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.55500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.14250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.92150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.55500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -125.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 CYS A 297
REMARK 465 PRO A 298
REMARK 465 GLN A 340
REMARK 465 HIS A 341
REMARK 465 THR A 342
REMARK 465 ARG A 343
REMARK 465 LYS A 344
REMARK 465 PRO A 345
REMARK 465 GLU A 346
REMARK 465 ASP A 347
REMARK 465 VAL A 348
REMARK 465 ARG A 349
REMARK 465 LYS A 717
REMARK 465 GLY A 718
REMARK 465 CYS B 297
REMARK 465 PRO B 298
REMARK 465 LYS B 344
REMARK 465 PRO B 345
REMARK 465 GLU B 346
REMARK 465 ASP B 347
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OH TYR B 706 O2D HEM B 801 2.08
REMARK 500 NE2 GLN B 364 O HOH B 901 2.13
REMARK 500 O HOH A 1016 O HOH A 1018 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 466 -78.64 -113.78
REMARK 500 SER A 491 -163.79 -77.48
REMARK 500 CYS A 582 57.74 -149.34
REMARK 500 ARG A 603 -134.54 -133.94
REMARK 500 CYS A 672 103.66 -160.10
REMARK 500 VAL A 715 98.62 -68.26
REMARK 500 ARG B 349 127.33 175.38
REMARK 500 SER B 392 -4.03 77.71
REMARK 500 LYS B 423 71.64 -107.17
REMARK 500 THR B 466 -84.21 -118.30
REMARK 500 CYS B 582 60.09 -150.95
REMARK 500 ARG B 603 -138.11 -123.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1021 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH B1087 DISTANCE = 5.97 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 805 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 326 SG
REMARK 620 2 CYS A 331 SG 114.1
REMARK 620 3 CYS B 326 SG 118.6 106.8
REMARK 620 4 CYS B 331 SG 106.6 98.6 110.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 801 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 415 SG
REMARK 620 2 HEM A 801 NA 104.0
REMARK 620 3 HEM A 801 NB 103.6 87.0
REMARK 620 4 HEM A 801 NC 99.5 156.5 88.6
REMARK 620 5 HEM A 801 ND 103.7 84.8 152.6 88.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 801 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 415 SG
REMARK 620 2 HEM B 801 NA 99.7
REMARK 620 3 HEM B 801 NB 104.7 86.4
REMARK 620 4 HEM B 801 NC 99.6 160.6 87.9
REMARK 620 5 HEM B 801 ND 99.0 86.4 156.1 91.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KN4 A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue H4B B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KN4 B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 806
DBREF 6NGY A 297 718 UNP P29476 NOS1_RAT 297 718
DBREF 6NGY B 297 718 UNP P29476 NOS1_RAT 297 718
SEQRES 1 A 422 CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR ASP
SEQRES 2 A 422 VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU
SEQRES 3 A 422 GLU THR GLY CYS THR GLU HIS ILE CYS MET GLY SER ILE
SEQRES 4 A 422 MET LEU PRO SER GLN HIS THR ARG LYS PRO GLU ASP VAL
SEQRES 5 A 422 ARG THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE
SEQRES 6 A 422 LEU ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER
SEQRES 7 A 422 LYS ALA HIS MET ASP ARG LEU GLU GLU VAL ASN LYS GLU
SEQRES 8 A 422 ILE GLU SER THR SER THR TYR GLN LEU LYS ASP THR GLU
SEQRES 9 A 422 LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER
SEQRES 10 A 422 ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL
SEQRES 11 A 422 PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE
SEQRES 12 A 422 ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS
SEQRES 13 A 422 GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG
SEQRES 14 A 422 THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN
SEQRES 15 A 422 LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER
SEQRES 16 A 422 THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE
SEQRES 17 A 422 CYS ILE GLN GLN GLY TRP LYS ALA PRO ARG GLY ARG PHE
SEQRES 18 A 422 ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP
SEQRES 19 A 422 PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU
SEQRES 20 A 422 VAL PRO ILE ARG HIS PRO LYS PHE ASP TRP PHE LYS ASP
SEQRES 21 A 422 LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN
SEQRES 22 A 422 MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS
SEQRES 23 A 422 PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL
SEQRES 24 A 422 ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU
SEQRES 25 A 422 GLU VAL ALA LYS LYS MET ASP LEU ASP MET ARG LYS THR
SEQRES 26 A 422 SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN
SEQRES 27 A 422 ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR
SEQRES 28 A 422 ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS
SEQRES 29 A 422 HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO
SEQRES 30 A 422 ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER
SEQRES 31 A 422 ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG
SEQRES 32 A 422 LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN
SEQRES 33 A 422 THR HIS VAL TRP LYS GLY
SEQRES 1 B 422 CYS PRO ARG PHE LEU LYS VAL LYS ASN TRP GLU THR ASP
SEQRES 2 B 422 VAL VAL LEU THR ASP THR LEU HIS LEU LYS SER THR LEU
SEQRES 3 B 422 GLU THR GLY CYS THR GLU HIS ILE CYS MET GLY SER ILE
SEQRES 4 B 422 MET LEU PRO SER GLN HIS THR ARG LYS PRO GLU ASP VAL
SEQRES 5 B 422 ARG THR LYS ASP GLN LEU PHE PRO LEU ALA LYS GLU PHE
SEQRES 6 B 422 LEU ASP GLN TYR TYR SER SER ILE LYS ARG PHE GLY SER
SEQRES 7 B 422 LYS ALA HIS MET ASP ARG LEU GLU GLU VAL ASN LYS GLU
SEQRES 8 B 422 ILE GLU SER THR SER THR TYR GLN LEU LYS ASP THR GLU
SEQRES 9 B 422 LEU ILE TYR GLY ALA LYS HIS ALA TRP ARG ASN ALA SER
SEQRES 10 B 422 ARG CYS VAL GLY ARG ILE GLN TRP SER LYS LEU GLN VAL
SEQRES 11 B 422 PHE ASP ALA ARG ASP CYS THR THR ALA HIS GLY MET PHE
SEQRES 12 B 422 ASN TYR ILE CYS ASN HIS VAL LYS TYR ALA THR ASN LYS
SEQRES 13 B 422 GLY ASN LEU ARG SER ALA ILE THR ILE PHE PRO GLN ARG
SEQRES 14 B 422 THR ASP GLY LYS HIS ASP PHE ARG VAL TRP ASN SER GLN
SEQRES 15 B 422 LEU ILE ARG TYR ALA GLY TYR LYS GLN PRO ASP GLY SER
SEQRES 16 B 422 THR LEU GLY ASP PRO ALA ASN VAL GLN PHE THR GLU ILE
SEQRES 17 B 422 CYS ILE GLN GLN GLY TRP LYS ALA PRO ARG GLY ARG PHE
SEQRES 18 B 422 ASP VAL LEU PRO LEU LEU LEU GLN ALA ASN GLY ASN ASP
SEQRES 19 B 422 PRO GLU LEU PHE GLN ILE PRO PRO GLU LEU VAL LEU GLU
SEQRES 20 B 422 VAL PRO ILE ARG HIS PRO LYS PHE ASP TRP PHE LYS ASP
SEQRES 21 B 422 LEU GLY LEU LYS TRP TYR GLY LEU PRO ALA VAL SER ASN
SEQRES 22 B 422 MET LEU LEU GLU ILE GLY GLY LEU GLU PHE SER ALA CYS
SEQRES 23 B 422 PRO PHE SER GLY TRP TYR MET GLY THR GLU ILE GLY VAL
SEQRES 24 B 422 ARG ASP TYR CYS ASP ASN SER ARG TYR ASN ILE LEU GLU
SEQRES 25 B 422 GLU VAL ALA LYS LYS MET ASP LEU ASP MET ARG LYS THR
SEQRES 26 B 422 SER SER LEU TRP LYS ASP GLN ALA LEU VAL GLU ILE ASN
SEQRES 27 B 422 ILE ALA VAL LEU TYR SER PHE GLN SER ASP LYS VAL THR
SEQRES 28 B 422 ILE VAL ASP HIS HIS SER ALA THR GLU SER PHE ILE LYS
SEQRES 29 B 422 HIS MET GLU ASN GLU TYR ARG CYS ARG GLY GLY CYS PRO
SEQRES 30 B 422 ALA ASP TRP VAL TRP ILE VAL PRO PRO MET SER GLY SER
SEQRES 31 B 422 ILE THR PRO VAL PHE HIS GLN GLU MET LEU ASN TYR ARG
SEQRES 32 B 422 LEU THR PRO SER PHE GLU TYR GLN PRO ASP PRO TRP ASN
SEQRES 33 B 422 THR HIS VAL TRP LYS GLY
HET HEM A 801 43
HET H4B A 802 17
HET KN4 A 803 26
HET ACT A 804 4
HET ZN A 805 1
HET HEM B 801 43
HET H4B B 802 17
HET KN4 B 803 26
HET ACT B 804 4
HET GOL B 805 6
HET GOL B 806 6
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM H4B 5,6,7,8-TETRAHYDROBIOPTERIN
HETNAM KN4 6-[2-(2,3-DIFLUORO-5-{2-[(2R)-1-METHYLPYRROLIDIN-2-
HETNAM 2 KN4 YL]ETHYL}PHENYL)ETHYL]-4-METHYLPYRIDIN-2-AMINE
HETNAM ACT ACETATE ION
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETSYN HEM HEME
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 H4B 2(C9 H15 N5 O3)
FORMUL 5 KN4 2(C21 H27 F2 N3)
FORMUL 6 ACT 2(C2 H3 O2 1-)
FORMUL 7 ZN ZN 2+
FORMUL 12 GOL 2(C3 H8 O3)
FORMUL 14 HOH *308(H2 O)
HELIX 1 AA1 THR A 315 SER A 320 5 6
HELIX 2 AA2 LYS A 351 ILE A 369 1 19
HELIX 3 AA3 SER A 374 SER A 392 1 19
HELIX 4 AA4 LYS A 397 ASN A 411 1 15
HELIX 5 AA5 GLY A 417 LEU A 424 5 8
HELIX 6 AA6 THR A 434 ASN A 451 1 18
HELIX 7 AA7 LYS A 452 ASN A 454 5 3
HELIX 8 AA8 ASN A 498 GLN A 507 1 10
HELIX 9 AA9 PRO A 537 VAL A 541 5 5
HELIX 10 AB1 TRP A 553 GLY A 558 5 6
HELIX 11 AB2 MET A 589 VAL A 595 1 7
HELIX 12 AB3 VAL A 595 ASP A 600 1 6
HELIX 13 AB4 ILE A 606 ASP A 615 1 10
HELIX 14 AB5 LYS A 620 SER A 623 5 4
HELIX 15 AB6 LEU A 624 ASP A 644 1 21
HELIX 16 AB7 ASP A 650 GLY A 670 1 21
HELIX 17 AB8 ASP A 675 VAL A 680 1 6
HELIX 18 AB9 SER A 684 THR A 688 5 5
HELIX 19 AC1 ASP A 709 HIS A 714 1 6
HELIX 20 AC2 THR B 315 SER B 320 5 6
HELIX 21 AC3 PRO B 338 THR B 342 5 5
HELIX 22 AC4 THR B 350 ILE B 369 1 20
HELIX 23 AC5 SER B 374 SER B 392 1 19
HELIX 24 AC6 LYS B 397 ASN B 411 1 15
HELIX 25 AC7 GLY B 417 TRP B 421 5 5
HELIX 26 AC8 THR B 434 ASN B 451 1 18
HELIX 27 AC9 LYS B 452 ASN B 454 5 3
HELIX 28 AD1 ASN B 498 GLN B 508 1 11
HELIX 29 AD2 PRO B 537 VAL B 541 5 5
HELIX 30 AD3 PHE B 551 GLY B 558 5 8
HELIX 31 AD4 GLY B 590 VAL B 595 1 6
HELIX 32 AD5 VAL B 595 ASP B 600 1 6
HELIX 33 AD6 ILE B 606 ASP B 615 1 10
HELIX 34 AD7 LYS B 620 SER B 623 5 4
HELIX 35 AD8 LEU B 624 ASP B 644 1 21
HELIX 36 AD9 ASP B 650 GLY B 670 1 21
HELIX 37 AE1 ASP B 675 VAL B 680 1 6
HELIX 38 AE2 SER B 684 THR B 688 5 5
HELIX 39 AE3 ASP B 709 HIS B 714 1 6
SHEET 1 AA1 2 LEU A 301 LYS A 304 0
SHEET 2 AA1 2 VAL A 311 ASP A 314 -1 O ASP A 314 N LEU A 301
SHEET 1 AA2 4 GLN A 425 ASP A 428 0
SHEET 2 AA2 4 ALA A 458 ILE A 461 1 O ILE A 459 N PHE A 427
SHEET 3 AA2 4 PHE A 584 SER A 585 -1 O SER A 585 N ALA A 458
SHEET 4 AA2 4 ALA A 566 VAL A 567 -1 N VAL A 567 O PHE A 584
SHEET 1 AA3 3 ARG A 473 VAL A 474 0
SHEET 2 AA3 3 LEU A 522 GLN A 525 -1 O GLN A 525 N ARG A 473
SHEET 3 AA3 3 GLU A 532 PHE A 534 -1 O PHE A 534 N LEU A 522
SHEET 1 AA4 2 GLY A 484 LYS A 486 0
SHEET 2 AA4 2 THR A 492 GLY A 494 -1 O LEU A 493 N TYR A 485
SHEET 1 AA5 2 GLU A 543 PRO A 545 0
SHEET 2 AA5 2 LYS A 560 TYR A 562 -1 O TRP A 561 N VAL A 544
SHEET 1 AA6 3 LEU A 577 PHE A 579 0
SHEET 2 AA6 3 LEU A 571 ILE A 574 -1 N LEU A 572 O PHE A 579
SHEET 3 AA6 3 SER A 703 GLU A 705 -1 O GLU A 705 N LEU A 571
SHEET 1 AA7 2 LEU B 301 LYS B 304 0
SHEET 2 AA7 2 VAL B 311 ASP B 314 -1 O ASP B 314 N LEU B 301
SHEET 1 AA8 4 GLN B 425 ASP B 428 0
SHEET 2 AA8 4 ALA B 458 ILE B 461 1 O ILE B 459 N PHE B 427
SHEET 3 AA8 4 PHE B 584 SER B 585 -1 O SER B 585 N ALA B 458
SHEET 4 AA8 4 ALA B 566 VAL B 567 -1 N VAL B 567 O PHE B 584
SHEET 1 AA9 3 ARG B 473 VAL B 474 0
SHEET 2 AA9 3 LEU B 522 GLN B 525 -1 O GLN B 525 N ARG B 473
SHEET 3 AA9 3 GLU B 532 PHE B 534 -1 O PHE B 534 N LEU B 522
SHEET 1 AB1 2 GLY B 484 LYS B 486 0
SHEET 2 AB1 2 THR B 492 GLY B 494 -1 O LEU B 493 N TYR B 485
SHEET 1 AB2 2 GLU B 543 PRO B 545 0
SHEET 2 AB2 2 LYS B 560 TYR B 562 -1 O TRP B 561 N VAL B 544
SHEET 1 AB3 3 LEU B 577 PHE B 579 0
SHEET 2 AB3 3 LEU B 571 ILE B 574 -1 N LEU B 572 O PHE B 579
SHEET 3 AB3 3 SER B 703 GLU B 705 -1 O GLU B 705 N LEU B 571
SHEET 1 AB4 2 TYR B 588 MET B 589 0
SHEET 2 AB4 2 ILE B 648 VAL B 649 1 O VAL B 649 N TYR B 588
LINK SG CYS A 326 ZN ZN A 805 1555 1555 2.44
LINK SG CYS A 331 ZN ZN A 805 1555 1555 2.44
LINK SG CYS A 415 FE HEM A 801 1555 1555 2.34
LINK ZN ZN A 805 SG CYS B 326 1555 1555 2.42
LINK ZN ZN A 805 SG CYS B 331 1555 1555 2.43
LINK SG CYS B 415 FE HEM B 801 1555 1555 2.37
CISPEP 1 THR A 701 PRO A 702 0 3.60
CISPEP 2 THR B 701 PRO B 702 0 0.88
SITE 1 AC1 13 TRP A 409 ALA A 412 ARG A 414 CYS A 415
SITE 2 AC1 13 PHE A 584 SER A 585 TRP A 587 TYR A 706
SITE 3 AC1 13 H4B A 802 KN4 A 803 ACT A 804 HOH A 903
SITE 4 AC1 13 HOH A 927
SITE 1 AC2 15 SER A 334 ARG A 596 VAL A 677 TRP A 678
SITE 2 AC2 15 HEM A 801 KN4 A 803 HOH A 927 HOH A 949
SITE 3 AC2 15 HOH A 977 HOH A 986 TRP B 676 PHE B 691
SITE 4 AC2 15 HIS B 692 GLN B 693 GLU B 694
SITE 1 AC3 12 MET A 336 VAL A 567 MET A 570 PHE A 584
SITE 2 AC3 12 SER A 585 GLY A 586 TRP A 587 TYR A 588
SITE 3 AC3 12 GLU A 592 TYR A 706 HEM A 801 H4B A 802
SITE 1 AC4 2 TRP A 587 HEM A 801
SITE 1 AC5 4 CYS A 326 CYS A 331 CYS B 326 CYS B 331
SITE 1 AC6 15 HIS B 341 TRP B 409 ARG B 414 CYS B 415
SITE 2 AC6 15 PHE B 584 SER B 585 GLY B 586 TRP B 587
SITE 3 AC6 15 GLU B 592 TRP B 678 TYR B 706 H4B B 802
SITE 4 AC6 15 KN4 B 803 HOH B 907 HOH B 909
SITE 1 AC7 14 TRP A 676 PHE A 691 HIS A 692 GLN A 693
SITE 2 AC7 14 GLU A 694 SER B 334 ARG B 596 VAL B 677
SITE 3 AC7 14 TRP B 678 HEM B 801 KN4 B 803 HOH B 909
SITE 4 AC7 14 HOH B 959 HOH B 999
SITE 1 AC8 10 MET B 336 VAL B 567 MET B 570 PHE B 584
SITE 2 AC8 10 GLY B 586 TRP B 587 GLU B 592 HEM B 801
SITE 3 AC8 10 H4B B 802 HOH B 909
SITE 1 AC9 3 GLY B 417 TRP B 587 HOH B 943
SITE 1 AD1 4 THR B 492 GLY B 494 ARG B 516 TYR B 604
SITE 1 AD2 5 LYS B 319 GLN B 364 ARG B 669 HOH B 906
SITE 2 AD2 5 HOH B 935
CRYST1 51.843 111.110 164.285 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.019289 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009000 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006087 0.00000
(ATOM LINES ARE NOT SHOWN.)
END